Virus Name | Equine Arteritis Virus |
Virus Short Name | EAV |
Order | Nidovirales |
Virus Family | Arteriviridae |
Virus Subfamily | N.A. |
Genus | Equartevirus |
Species | Equine Arteritis Virus |
Host | Vertebrates |
Cell Tropism | Primarily lung macrophages and later in lymph nodes |
Associated Disease | Vascular lesions, fever, edema, abortion |
Mode of Transmission | Genital and respiratory tract secretions. |
VIPR DB link | N.A. |
ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/positive-sense-rna-viruses-2011/w/posrna_viruses/220/arteriviridae |
Virus Host DB link | N.A. |
Paper Title | Equine arteritis virus non-structural protein 1, an essential factor for viral subgenomic mRNA synthesis, interacts with the cellular transcription co-factor p100 |
Author's Name | Marieke A. Tijms and Eric J. Snijder |
Journal Name | Journal of General Virology |
Pubmed ID | 12917451 |
Abstract | Non-structural protein 1 (nsp1), the N-terminal subunit of the replicase polyprotein of the arterivirus Equine arteritis virus (EAV), is essential for viral subgenomic mRNA synthesis, but fully dispensable for genome replication. However, at the molecular level, the role of nsp1 in EAV subgenomic mRNA synthesis is poorly understood. A yeast two-hybrid screen did not reveal interactions between EAV nsp1 and other viral non-structural proteins or the nucleocapsid protein, although both nsp1 and the nucleocapsid protein were found to form homomers. Subsequently, a yeast two-hybrid screen of a HeLa cell cDNA library was performed using nsp1 as bait. Remarkably, this analysis revealed (potential) interactions between EAV nsp1 and factors that are involved in host cell transcriptional regulation. The interaction of nsp1 with one of these proteins, p100, a transcription co-activator that also interacts with regulatory proteins of other viruses, was confirmed by mutual co-immunoprecipitation from lysates of EAV-susceptible mammalian cells. |
Used Model | HeLa cell |
DOI | 10.1099/vir.0.19297-0 |